Abstract: Antibodies directed against an antigenic determinant of high molecular weight kininogen domain 5, particularly a determinant located in the region formed by light chain amino acids Gly(440) to Lys(502), inhibit angiogenesis.

Abstract: Antibodies directed against an antigenic determinant of high molecular weight kininogen domain 5, particularly a determinant located in the region formed by light chain amino acids Gly(440) to Lys(502), inhibit angiogenesis.

Abstract: Peptide analogs of the high molecular weight kininogen domain 5 are potent inhibitors of angiogenesis. The peptides have the formula X1-(HGLGHGHEQQHGKGH)-X2  (I) wherein X1 is from zero to 25 amino acids; X2 is from zero to 60 amino acids. Methods of inhibiting endothelial cell proliferation and angiogenesis are provided.

Abstract: Synthetic peptide analogs of human kininogen are provided which are conformationally restricted by means of intramolecular bonding. The peptides mimic the biological activity of human kininogen by inhibiting the activity of the biologically significant protease, calpain. The peptides are designed by means of an equilibrium conformational model of the kininogen heavy chain.

Abstract: Synthetic peptide analogs of human kininogen are provided which are conformationally restricted by means of intramolecular bonding. The peptides mimic the biological activity of human kininogen by inhibiting the activity of the biologically significant protease, calpain. The peptides are designed by means of an equilibrium conformational model of the kininogen heavy chain.

Abstract: Four novel cell lines, ATCC #HB-8862 through ATCC #HB-8865 produce monoclonal antibody to human plasma prekallikrein. At least three of the antibodies also recognize plasma kallikrein, specifically the heavy chain thereof, and kallikrein-Cl-inhibitor complex; at least one of these three antibodies recognizes kallikrein-alpha.sub.2 -macroglobulin complex and kallikrein-antithrombin III complex. The antibodies do not cross-react with tissue kallikrein. The hybridomas are formed by fusing spleen cells from immunized BALB/c AnSkh mice with SP2/O-Agl4 myeloma cells. Diagnostic and biochemical uses of the monoclonal antibodies are provided.

Abstract: This invention provides a method of inhibiting coagulation in extracorporeal circulation in a subject, comprising administration of a therapeutically effective amount of a monoclonal antibody which inhibits the ability of tissue factor to bind to factor VII/VIIa. The method prevents complex formation between tissue factor and factor VII/VIIa and thus inhibits coagulation of blood in extracorporeal procedures such as cardiopulmonary bypass and other shunt procedures. Anti-tissue factor monoclonal antibodies produced by hybridoma cell lines TFS-5G9 or TF9-6B4 may be used in the claimed methods.

Abstract: Peptides and pharmaceutically acceptable salts thereof of the following formula are provided ##STR1## wherein R is selected from the group consisting of Leu, Ile and Val,X is from zero to four amino acids,Y is from zero to four amino acids, andZ is OH or NH.sub.2.The compounds are useful in inhibiting thrombin- and plasmin-induced aggregation of human platelets.

Abstract: Two novel cell lines, ATCC #HB-8963 and ATCC #HB-8964 produce monoclonal antibody to human kininogen. One of the antibodies specifically recognizes the heavy chain of high and low molecular weight kininogen (the later protein is identical to alpha cysteine protease inhibitor). The other antibody recognizes the light chain of high molecular weight kininogen. The hybridomas are formed by fusing spleen cells from immunized BALB/c AnSkh mice with P3X63Ag8 or SP2/0-Ag14 myeloma cells. Diagnostic, therapeutic and biochemical uses of the monoclonal antibodies are provided.

Abstract: Two novel cell lines, ATCC #HB-8963 and ATCC #HB-8964 produce monoclonal antibody to human kininogen. One of the antibodies specifically recognizes the heavy chain of high and low molecular weight kininogen (the later protein is identical to alpha cysteine protease inhibitor). The other antibody recognizes the light chain of high molecular weight kininogen. The hybridomas are formed by fusing spleen cells from immunized BALB/c AnSkh mice with P3X63Ag8 or SP2/0-Ag14 myeloma cells. Diagnostic, therapeutic and biochemical uses of the monoclonal antibodies are provided.

Abstract: An assay for functional high molecular weight kininogen in plasma is provided. A plasma sample of unknown functional high molecular kininogen content is treated to inactivate plasma protease inhibitors and kallikrein, and is appropriately neutralized and diluted. Exogenous factor XIIa and factor XI are added to the sample to form a reaction mixture which is incubated with a contact-activating surface. The concentrations of factor XIIa and factor XI in the reaction mixture are selected such that the concentration of functional high molecular weight kininogen in the sample is rate-limiting in the HMWK-mediated activation of factor XI by factor XIIa. The amount of factor XIa generated in the sample, which under the conditions of the assay is directly proportional to the concentration of functional HMWK, may be determined by functional assay using an appropriate factor XIa substrate.